Human coagulation factor VIII domain-specific recombinant polypeptide expression.

ABSTRACT:

Background

Hemophilia A is caused by heterogeneous mutations in F8. Coagulation factor VIII (FVIII), the product of F8, is composed of multiple domains designated A1-A2-B-A3-C1-C2. FVIII is known to interact with diverse proteins, and this characteristic may be important for hemostasis. However, little is known about domain-specific functions or their specific binding partners.

Methods

To determine F8 domain-specific functions during blood coagulation, the FVIII domains A1, A2, A3, and C were cloned from Hep3B hepatocytes. Domain-specific recombinant polypeptides were glutathione S-transferase (GST)- or polyhistidine (His)-tagged, over-expressed in bacteria, and purified by specific affinity chromatography.

Results

Recombinant polypeptides of predicted sizes were obta

SUBMITTER: Choi SJ 

PROVIDER: S-EPMC4486152 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature